A beta 3 integrin mutation abolishes ligand binding and alters divalent cation-dependent conformation.
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Loftus JC, O'Toole TE, Plow EF, Glass A, Frelinger AL 3rd, Ginsberg MH
A beta 3 integrin mutation abolishes ligand binding and alters divalent cation-dependent conformation.
Science. 1990 Aug 24;249(4971):915-8.
- PubMed ID
- 2392682 [ View in PubMed]
- Abstract
The ligand-binding function of integrin adhesion receptors depends on divalent cations. A mutant alpha IIb beta 3 integrin (platelet gpIIb/IIIa) that lacks ligand recognition shows immunologic evidence of a perturbed interaction with divalent cations. This was found to be caused by a G----T mutation that resulted in an Asp119----Tyr119 substitution in the beta 3 subunit. This residue is proximal to bound ligand and is in a conserved region among integrins that are enriched in oxygenated residues. The spacing of these residues aligns with the calcium-binding residues in EF hand proteins, suggesting interaction with receptor-bound divalent cation as a mechanism of ligand binding common to all integrins.